ID   MSK2_MEDSA              Reviewed;         411 AA.
AC   P51138;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Glycogen synthase kinase-3 homolog MsK-2;
DE            EC=2.7.11.1;
GN   Name=MSK-2;
OS   Medicago sativa (Alfalfa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8401615; DOI=10.1111/j.1365-313x.1993.00847.x;
RA   Paz A., Jonak C., Boegre L., Meskiene I., Mairinger T., Szalay A.,
RA   Heberle-Bors E., Hirt H.;
RT   "The MsK family of alfalfa protein kinase genes encodes homologues of
RT   shaggy/glycogen synthase kinase-3 and shows differential expression
RT   patterns in plant organs and development.";
RL   Plant J. 3:847-856(1993).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1;
CC   -!- TISSUE SPECIFICITY: Absent in leaves and petioles while a moderate
CC       expression is seen in the stems, roots, and nodes.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. GSK-3 subfamily. {ECO:0000305}.
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DR   EMBL; X68410; CAA48473.1; -; mRNA.
DR   PIR; S37643; S37643.
DR   AlphaFoldDB; P51138; -.
DR   SMR; P51138; -.
DR   BRENDA; 2.7.11.26; 3078.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   CDD; cd14137; STKc_GSK3; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR039192; STKc_GSK3.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..411
FT                   /note="Glycogen synthase kinase-3 homolog MsK-2"
FT                   /id="PRO_0000086401"
FT   DOMAIN          74..358
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        199
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         80..88
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         103
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         234
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   411 AA;  46062 MW;  BBB0CA647633989E CRC64;
     MATAGVAPAS GIVDVNASSA IAVDKLPDEI LGMRIKDDKE MEAHVVDGNS TEAGHVIVTT
     IGGKNGQPKQ TISYMAERAV GQGSFGVVFQ AKCLETGETV AIKKVLQDKR YKNRELQTMR
     LLDHPNVVTL KHCFFSTTEK DELYLNLVLE FVPETVHRVI RHYSKMNQRM PLIYVKLYSY
     QICRSLAYIH NCVGVSHRDI KPQNLLVNPH THQLKLCDFG SAKVLVKGEP NISYICSRYY
     RAPELIFGAT EYTSAIDIWS AGCVLGELLL GQPLFPGASG VDQLVEIIKV LGTPTREEIK
     CMNPNYTEFK FPQIKAHPWH KIFRKRMPPE AVDLVSRLLQ YSPNLRSTAL EALVHPFFDE
     LRDPNTRLPN GRHLPPLFNF KANELKGVPA EMLVKLVPSH ARKQCSLFAS S